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The uptake of zinc by selected mushroom fungi.January 1994 (has links)
Sandra J. Chapman. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1994. / Includes bibliographical references (leaves 95-103). / Chapter 1. --- Introduction --- p.1 / Chapter 1.1 --- History of zinc --- p.1 / Chapter 1.2 --- The biological role of zinc --- p.2 / Chapter 1.3 --- Zinc toxicosis --- p.6 / Chapter 1.4 --- Mechanisms of zinc uptake and transport in fungi --- p.7 / Chapter 1.5 --- Bioremediation --- p.11 / Chapter 1.6 --- Uptake of heavy metals by fruit bodies of edible mushrooms --- p.13 / Chapter 1.7 --- Mushroom fungi selected for study --- p.15 / Chapter 1.8 --- Purpose of study --- p.17 / Chapter 2. --- Materials and Methods --- p.18 / Chapter 2.1 --- Organisms --- p.18 / Chapter 2.2 --- Media --- p.18 / Chapter 2.3 --- Media chelation --- p.20 / Chapter 2.4 --- Chemicals --- p.20 / Chapter 2.5 --- Zinc content of fruit bodies grown on substrates containing different concentrations of zinc --- p.21 / Chapter 2.5.1 --- Substrate preparation for V. volvacea inoculum --- p.21 / Chapter 2.5.2 --- Cultivation of V. volvacea fruit bodies --- p.21 / Chapter 2.5.3 --- Cultivation of P.sajor-caju fruit bodies --- p.22 / Chapter 2.5.4 --- Cultivation of L. edodes fruit bodies --- p.23 / Chapter 2.5.5 --- Preparation of biological material for atomic absorption spectrophotometry --- p.24 / Chapter 2.6 --- Effect of different concentrations of zinc on the growth of six mushroom fungi --- p.25 / Chapter 2.6.1 --- Radial growth study --- p.25 / Chapter 2.6.2 --- Biomass study --- p.26 / Chapter 2.7 --- Microscopic studies of V. volvacea --- p.27 / Chapter 2.7.1 --- "Coomassie Blue preparation, staining of V.volvacea hyphae" --- p.27 / Chapter 2.7.2 --- Dithizone staining of V. volvacea hyphae --- p.27 / Chapter 2.7.3 --- Fluorescence microscopy --- p.28 / Chapter 2.7.4 --- Scanning electron microscopy --- p.28 / Chapter 2.8 --- Preparation and analysis of V. volvacea proteins using gel electrophoresis --- p.29 / Chapter 3. --- Results --- p.33 / Chapter 3.1 --- Zinc Uptake by Fruit Bodies --- p.33 / Chapter 3.1.1 --- Uptake of zinc by V. volvacea --- p.33 / Chapter 3.1.2 --- Uptake of zinc by P. sajor-caju --- p.33 / Chapter 3.1.3 --- Uptake of zinc by L. edodes --- p.34 / Chapter 3.1.4 --- Symptoms of zinc toxicity in L. edodes --- p.44 / Chapter 3.2 --- Growth studies --- p.49 / Chapter 3.2.1 --- Radial growth measurements --- p.49 / Chapter 3.2.2 --- Biomass measurements --- p.56 / Chapter 3.2.3 --- Morphological alterations due to zinc observed with light and electron microscopy --- p.63 / Chapter 3.3 --- V. volvacea staining studies --- p.73 / Chapter 3.3.1 --- Protein staining using Coomassie Blue --- p.73 / Chapter 3.3.2 --- Zinc staining by dithizone and fluorescence staining by DAPI --- p.75 / Chapter 3.4 --- V. volvacea protein profile comparisons after gel electrophoresis --- p.81 / Chapter 4. --- Discussion --- p.83 / Chapter 4.1 --- Zinc uptake by fruit bodies / Chapter 4.1.1 --- Uptake of zinc by V. volvacea and P. sajor-caju fruit bodies --- p.83 / Chapter 4.1.2 --- Accumulation of zinc by L. edodes fruit bodies and mechanism of toxicity --- p.84 / Chapter 4.2 --- Effects of zinc on growth --- p.88 / Chapter 4.3 --- V. volvacea mechanisms of tolerance --- p.89 / Chapter 4.4 --- Differences in protein profiles of V. volvacea grown on different concentrations of zinc --- p.93 / Chapter 5. --- References
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Cellulolytic and hemicellulolytic enzymes of flammulina velutipes.January 1994 (has links)
by Cheung Pui Yi. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1994. / Includes bibliographical references (leaves 124-135). / Abstract --- p.ii / Acknowledgements --- p.iv / List of Tables --- p.viii / List of Figures --- p.ix / List of Abbreviations --- p.xiii / Chapter Chapter 1 --- Introduction / Chapter 1.1 --- General Background --- p.1 / Chapter 1.2 --- Occurrence and Structure of Cellulose --- p.1 / Chapter 1.3 --- Occurrence and Structure of Hemicelluloses --- p.4 / Chapter 1.4 --- Biodegradation of Cellulose and Hemicelluloses --- p.4 / Chapter 1.4.1 --- Cellulolytic and Hemicellulolytic Microorganisms --- p.4 / Chapter 1.4.2 --- Enzymes Involved in Cellulose Degradation --- p.10 / Chapter 1.4.2.1 --- "Endo-1,4-β-glucanases" --- p.12 / Chapter 1.4.2.2 --- "Exo-1,4-β-glucanases" --- p.14 / Chapter 1.4.2.3 --- β-Glucosidases --- p.16 / Chapter 1.4.2.4 --- Oxidative Enzymes --- p.18 / Chapter 1.4.3 --- Synergistic Action between Cellulolytic Enzymes --- p.19 / Chapter 1.4.4 --- Enzymes Involved in Hemicellulose Degradation --- p.21 / Chapter 1.4.4.1 --- "Endo-1,4-β-xylanases" --- p.22 / Chapter 1.4.4.2 --- β-Xylosidases --- p.24 / Chapter 1.4.4.3 --- Other Xylanolytic Enzymes --- p.24 / Chapter 1.4.5 --- Synergistic Action between Hemicellulolytic Enzymes --- p.25 / Chapter 1.5 --- Flammulina velutipes --- p.26 / Chapter 1.6 --- Aims of the Present Investigation --- p.27 / Chapter Chapter 2 --- Materials and Methods / Chapter 2.1 --- Organism --- p.28 / Chapter 2.2 --- Culture Medium --- p.28 / Chapter 2.3 --- Determination of the Optimal Growth pH of Flammulina velutipes --- p.29 / Chapter 2.4 --- "Preparation of Inoculum, Cultivation and Harvest of Fungal Cultures" --- p.30 / Chapter 2.5 --- Enzyme Assays --- p.30 / Chapter 2.5.1 --- "Exo-1,4-β-glucanase" --- p.30 / Chapter 2.5.2 --- "Endo-1,4-β-glucanase" --- p.31 / Chapter 2.5.3 --- "Endo-1,4-β-xylanase" --- p.34 / Chapter 2.5.4 --- Extracellular β-Glucosidase --- p.36 / Chapter 2.5.5 --- Cell-Associated β-Glucosidase --- p.38 / Chapter 2.5.6 --- Extracellular β-Xylosidase --- p.38 / Chapter 2.5.7 --- Cell-Associated β-Xylosidase --- p.38 / Chapter 2.6 --- Determination of Optimal Temperatures for Cellulolytic and Xylanolytic Enzymes --- p.39 / Chapter 2.7 --- Determination of the Optimal pH for Enzyme Reaction --- p.39 / Chapter 2.8 --- Protein Determination --- p.39 / Chapter 2.9 --- Determination of Enzyme Induction Patterns --- p.42 / Chapter 2.10 --- Elucidation of Cellulase Production Patterns in F. velutipes --- p.43 / Chapter 2.10.1 --- Native Polyacrylamide Gel Electrophoresis --- p.43 / Chapter 2.10.2 --- Activity Staining for Endoglucanases --- p.43 / Chapter 2.10.3 --- Activity Staining for β-Glucosidases --- p.44 / Chapter 2.10.4 --- Protein Staining --- p.44 / Chapter 2.10.5 --- Preparative Polyacrylamide Gel Electrophoresis --- p.44 / Chapter 2.10.6 --- Separation of Proteins and Partial Purification of Different Cellulase Species after Preparative Polyacrylamide Gel Electrophoresis --- p.45 / Chapter Chapter 3 --- Results / Chapter 3.1 --- Determination of the Optimal pH for Fungal Growth --- p.46 / Chapter 3.2 --- Determination of the Optimal Temperature for Cellulolytic and Xylanolytic Enzyme Activity --- p.48 / Chapter 3.3 --- Determination of the Optimal pH for Enzyme Reaction --- p.64 / Chapter 3.4 --- Time Course Experiments on the Production of Cellulolytic and Hemicellulolytic Enzymes --- p.72 / Chapter 3.4.1 --- Production of Cellulolytic Enzymes --- p.72 / Chapter 3.4.2 --- Production of Hemicellulolytic Enzymes --- p.77 / Chapter 3.5 --- Determination of Enzyme Induction Patterns --- p.82 / Chapter 3.5.1 --- Induction of Exoglucanase Production --- p.82 / Chapter 3.5.2 --- Induction of Endoglucanase Production --- p.84 / Chapter 3.5.3 --- Induction of Extracellular β-Glucosidase Production --- p.86 / Chapter 3.5.4 --- Induction of β-Xylanase Production --- p.88 / Chapter 3.5.5 --- Induction of Extracellular β-Xylosidase Production --- p.90 / Chapter 3.5.6 --- Changes in Extracellular Protein Levels in DMS Media Supplemented with Different Substrates --- p.92 / Chapter 3.5.7 --- Changes in Reducing Sugar Levels in DMS Media Supplemented with Different Substrates --- p.94 / Chapter 3.6 --- Partial Purification of Different Cellulases Species Produced by Flammulina velutipes --- p.96 / Chapter 3.6.1 --- Native Polyacrylamide Gel Electrophoresis --- p.96 / Chapter 3.6.2 --- Activity Staining for Endoglucanases --- p.96 / Chapter 3.6.3 --- Activity Staining for β-Glucosidases --- p.96 / Chapter 3.6.4 --- Assay of Cellulolytic Enzymes after Preparative Polyacrylamide Gel Electrophoresis --- p.101 / Chapter Chapter 4 --- Discussion / Chapter 4.1 --- Optimal Conditions for Cellulolytic and Hemicellulolytic Enzymes of F. velutipes --- p.105 / Chapter 4.1.1 --- Optimal Temperature for Enzymic Reaction --- p.105 / Chapter 4.1.2 --- Optimal pH for Enzymic Reaction --- p.106 / Chapter 4.2 --- Production of Cellulolytic and Hemicellulolytic Enzymes --- p.109 / Chapter 4.2.1 --- Production of Cellulolytic Enzymes --- p.109 / Chapter 4.2.2 --- Production of Hemicellulolytic Enzymes --- p.110 / Chapter 4.3 --- Enzyme Induction Patterns --- p.111 / Chapter 4.4 --- Partial Purification of Different Cellulase Species Produced by Flammulina velutipes --- p.116 / Chapter 4.5 --- Conclusion --- p.121 / Chapter 4.6 --- Further Studies --- p.123 / List of References --- p.124
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